Folding and intrinsic stability of deletion variants of PrP(121-231), the folded C-terminal domain of the prion protein

Biophysical Chemistry

Volumn 96, Issue 2-3, 2002, Pages 293-303

  Eberl, Heike ^a   Glockshuber, Rudi ^a  

^a ETH ZURICH   (Switzerland)

Author keywords

Deletion variants; Prion protein; Stability; Structure of PrPSc

Indexed keywords

ASPARAGINE; DIPEPTIDE; GLYCINE; PRION PROTEIN; RECOMBINANT PROTEIN; BACTERIAL PROTEIN; PEPTIDE FRAGMENT; PHOSPHOPROTEIN PHOSPHATASE; PRION PROTEIN (121 231); PRION PROTEIN (121-231); PRPC PROTEIN, BACTERIAL; UREA;

ALPHA HELIX; ARTICLE; BETA SHEET; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; CONFORMATION; CONTROLLED STUDY; MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN VARIANT; THERMODYNAMICS; ANIMAL; CHEMISTRY; DRUG EFFECT; GENE DELETION; GENETICS; MOUSE; PH; PRION; PROTEIN DENATURATION; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE;

MAMMALIA;

ANIMALS; BACTERIAL PROTEINS; CIRCULAR DICHROISM; HYDROGEN-ION CONCENTRATION; MICE; PEPTIDE FRAGMENTS; PHOSPHOPROTEIN PHOSPHATASE; PRIONS; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PRPSC PROTEINS; SEQUENCE DELETION; UREA;

EID: 0037007448     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(02)00015-7     Document Type: Article

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